ID A0A1V9XW12_9ACAR Unreviewed; 518 AA.
AC A0A1V9XW12;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JUN-2023, entry version 23.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE Flags: Fragment;
GN ORFNames=BIW11_06924 {ECO:0000313|EMBL:OQR77670.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR77670.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR77670.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR77670.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001593};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR77670.1}.
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DR EMBL; MNPL01003247; OQR77670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XW12; -.
DR STRING; 418985.A0A1V9XW12; -.
DR InParanoid; A0A1V9XW12; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR009398; Adcy_conserved_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF26; ADENYLATE CYCLASE TYPE 1; 1.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; Adcy_cons_dom; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 493..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..260
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 357..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 518
FT /evidence="ECO:0000313|EMBL:OQR77670.1"
SQ SEQUENCE 518 AA; 58810 MW; BF53B9BC7B4BAF6B CRC64;
MVCINLVGVI LHTLMEKAQR KAFLDTRNCI QARLDMEDEN ERLERLLLSV LPQHVAVEMK
KDIVNPRVTG QFHKIYIQKH ENVSILFADI VGFTVLSSHL PAPELVRLLN ELFGRFDQLA
NDNNCLRIKI LGDCYYCVSG LPERSDHAQC AVNMGLDMVD AIKEVGTLVF RCGHRPSYLA
VYDAPYFTHR EPRSTSTHTL SSSRMGRPEQ VAELMADFSA CSLNMRVGIH TGRVLCGVLG
LRKWQYDVWS NDVTLANQME AGGVPGRVHI TAATLKYLNN DFQVEPGRGE DRSAYLRDHG
VTTYFIVPPP NRHKKVIFNS IQMRRMTGRK LSFKNVSNVV VQLLHSIRFS VDVPFSNLNG
PPPSHHHQQQ HPGSHNAQQN SHHHPSHPSS FQQDNNNSDR VACLAAQLNP LMGVDKAGTN
NNNKKGKMDK FRKPFKKRHS EMYHQPTNRV NKYLSQAINA RSVDQEKSNH VNLLTLCFKD
DEKERRYHQE RDLGFVSSLA CALFISIFLS AFHLVILP
//
